Hydrophobicity of amino

Many scales, either empirical or measured, have been proposed for the hydrophobicity of amino acid residues in proteins (Nakai and Li-Chan, 1988). The most extensive study on tlje hydrophobicity index of amino acids was published by Wilce et al. (1995). The authors derived four new scales of coefficients from the reversed-phase high-performance liquid chromatographic retention data of 1738 peptides and compared them with 12 previously published scales. 

Figure 3. Taste intensity and hydrophobicity of amino acid...

Volume = Volume enclosed by van der Waals radii Mass = molecular weight of nonionized amino acid minus that of water both adopted from Creighton (1993) HP scale = degree of hydrophobicity of amino acid side chains, based on Kyte Doolittle (1982) Surface Area = mean fraction buried, based on Rose et al. (1985) and Secondary structure propensity = the normalized frequencies for each conformation, adopted from Creighton (1993), is the fraction of residues of each amino acid that occurred in that conformation, divided by this fraction for all residues. 

HINT), is a hydrophobic field calculated by -> Leo-Hansch hydrophobic fragmental constants scaled by surface area and a distance-dependent function [Kellogg et al., 1991 Kellogg and Abraham, 1992a Abraham and Kellogg, 1993]. Hydropathy is a term used in structural molecular biology to represent the hydrophobicity of amino acid side chains. 

G. D. Rose, A. R. Geselowitz, G. J. Lesser et al. Hydrophobicity of amino acid residues in globular proteins. Science, 229 (1985), 834 S. Miller, J. Janin, A. M. Lesk et al. Interior and surface of monomeric proteins. Journal of Molecular Biology, 196 (1987), 641 C. Lawrence, 1. Auger and C. Mannella. Distribution of accessible surfaces of amino acids in globular proteins. Proteins, 2 (1987), 153. 

Pacios, L.F. (2001) Distinct molecular surfaces and hydrophobicity of amino acid residues in proteins. J. Chem. Inf. Comput. Sci., 41, 1427—1435. 

M.J. Medina Hernandez, M. Catala Icardo and M.C. Garcia Alvarez-Coque, Correlation between Hydrophobicity of Amino Acids and Retention Data in RPLC with Micellar Eluents, Chromatographia, 41 455 (1995). 

Research on the physicochemical properties of A -acylamino acids has been periodic, except for the effort at Ajinimoto Company, lead primarily by Yoshida, Takehara, and Sakamoto. As a result, there are few systematic studies on the structure and property relationship of Af-acylamino acids. Sakamoto introduced the hydrophobicity of amino acid as a measure of such structure and activity relationship [48,49]. The hydrophobicity of each amino acid is proposed by Tanford as a free-energy change from ethyl alcohol to water and normalized to Gly, as shown by the Eq. (1) [50] (Table 2). 

The surface tension of the sodium salt of A -lauroylamino acids increased with the increase of hydrophobicity of amino acid, as shown in Fig. 7. There... 

The experimental observation that the retention time of amino acids derivatized with FDAA were dependent on the hydrophobicity of amino acids further confirms the proposed mechanism, for example, the FDAA derivative of an amino acid, which has a larger difference in hydrophobicity between the a -carboxyl group and the side chain, has a longer retention time and a better resolution. Separation behavior of FDAA derivatives of amino acid methyl esters and amino compounds without the a-carboxyl group, such as 1-phenylethylamine, alanilol, and valinol. 

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